| IED ID | IndEnz0001000423 |
| Enzyme Type ID | amylase000423 |
| Protein Name |
Beta-amylase EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase |
| Gene Name | BMY1 BA1 |
| Organism | Medicago sativa (Alfalfa) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Trifolieae Medicago (medics) Medicago sativa (Alfalfa) |
| Enzyme Sequence | MATSNKNMLLNYVPVYVMLPLGVINVNNVFEDPDGLKEQLVQLRAAGVDGVMIDVWWGIIEQKGPKEYDWSAYKSLFQLVQKCGLKLQAIMSFHQCGGNVGDVVNIPLPKWVLDIGESDPDIFYTNRSGIRNQEYLSIGVDNKPIFHGRTAIEIYSDYMKSFRENMSDLLKSEVIIDIEVGLGPAGELRYPSYPQNQGWQFPGIGEFQCYDKYLRESFKAAAAKAGHSEWELPDDAGTYNDVPESTEFFKTNGTYLTEKGKFFLTWYSNQLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKAPNHAAELTAGYYNLDDRDGYRPIAKIVSRHHAILNFTCLEMRDSEQSSDAHSSPQKLVQQVLSGGWRENIEVAGENALSRYDATAYNQIILNARPQGVNKDGPPKLRMYGVTYLRLSDDLMQQSNFDIFKKFVVKMHADQDYCSDPEKYNHGIPPLKRSGPKIPDDVLNEATKPIPPFPWDSETDMKVDG |
| Enzyme Length | 496 |
| Uniprot Accession Number | O22585 |
| Absorption | |
| Active Site | ACT_SITE 187; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 381; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10538 |
| Activity Regulation | |
| Binding Site | BINDING 54; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 94; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 102; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 296; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 301; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 343; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 421; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Region (2) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,140 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |